SRR Human

Serine Racemase Human Recombinant
Cat. No.
BT7357
Source
Escherichia Coli.
Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.
SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Serine racemase (SRR) is an enzyme that converts L-serine to D-serine. D-serine acts as a signaling molecule in neurons by activating NMDA receptors in the brain. In mammals, SRR is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes both the racemization of L-serine to D-serine and the dehydration of L-serine to pyruvate and ammonia. The activity of SRR is enhanced by divalent cations such as magnesium and is allosterically activated by the magnesium/ATP complex.
Description
Recombinant human SRR, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 364 amino acids (residues 1-340) with a molecular weight of 39.1 kDa. The protein is fused to a 24-amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The SRR solution is supplied at a concentration of 0.5 mg/ml in 20 mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.1 M NaCl, and 1 mM DTT.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product at -20°C. To ensure stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 85.0% as determined by SDS-PAGE analysis.
Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.

Product Science Overview

Introduction

Serine racemase (SR) is a pivotal enzyme in human biology, known for its unique ability to convert L-serine to its enantiomer, D-serine . This enzyme is encoded by the SRR gene located on chromosome 17 in humans . D-serine plays a crucial role as a neuronal signaling molecule by activating N-methyl-D-aspartate (NMDA) receptors in the brain .

Structure and Function

Serine racemase is a pyridoxal 5’-phosphate (PLP)-dependent enzyme that catalyzes two primary reactions:

  1. Racemization: Conversion of L-serine to D-serine.
  2. β-elimination: Conversion of L-serine to pyruvate and ammonia .

The enzyme’s activity is modulated by divalent cations such as magnesium and is allosterically activated by the magnesium/ATP complex . Key residues in the active site, including K56 and S84, play significant roles in PLP cofactor binding and activity modulation .

Biological Significance

D-serine, produced by serine racemase, acts as a co-agonist of NMDA receptors, which are essential for synaptic plasticity, memory formation, and learning . Dysfunction of NMDA receptors has been implicated in various neurological disorders, including schizophrenia . Underexpression of serine racemase has been associated with the paranoid subtype of schizophrenia, and treatment with D-serine has shown potential in ameliorating some symptoms .

Evolutionary Perspective

Serine racemase may have evolved from L-threo-hydroxyaspartate (L-THA) eliminase and served as a precursor to aspartate racemase . This evolutionary adaptation highlights the enzyme’s significance in amino acid metabolism and neuronal signaling.

Recombinant Human Serine Racemase

Recombinant human serine racemase is produced using advanced biotechnological methods to study its structure, function, and potential therapeutic applications. The recombinant form retains the enzyme’s native activity and is used in various research applications to understand its role in neurodegenerative diseases and to develop specific small molecule modulators .

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